{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,26]],"date-time":"2026-05-26T12:07:30Z","timestamp":1779797250300,"version":"3.53.1"},"reference-count":41,"publisher":"Springer Science and Business Media LLC","issue":"5","license":[{"start":{"date-parts":[[2025,9,10]],"date-time":"2025-09-10T00:00:00Z","timestamp":1757462400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2025,9,10]],"date-time":"2025-09-10T00:00:00Z","timestamp":1757462400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"funder":[{"DOI":"10.13039\/501100008386","name":"Marmara \u00dcniversitesi","doi-asserted-by":"publisher","award":["FDK-2022-10061"],"award-info":[{"award-number":["FDK-2022-10061"]}],"id":[{"id":"10.13039\/501100008386","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Mol Biotechnol"],"published-print":{"date-parts":[[2026,5]]},"DOI":"10.1007\/s12033-025-01500-x","type":"journal-article","created":{"date-parts":[[2025,9,10]],"date-time":"2025-09-10T16:46:15Z","timestamp":1757522775000},"page":"2410-2421","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Expression, Purification and Biochemical Characterisation of Babesia bigemina Lactate Dehydrogenase"],"prefix":"10.1007","volume":"68","author":[{"given":"Safiye Merve","family":"Bostancioglu","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ozkan","family":"Danis","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sinem","family":"Kocer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4551-5780","authenticated-orcid":false,"given":"Ozal","family":"Mutlu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2025,9,10]]},"reference":[{"key":"1500_CR1","doi-asserted-by":"crossref","unstructured":"Smith, T. and Kilborne, F. L. (1893) Investigations into the nature, causation, and prevention of Texas or southern cattle fever. Dept. of Agriculture, Bureau of Animal Industry, Washington D.C., U.S.","DOI":"10.5962\/bhl.title.124068"},{"issue":"Suppl","key":"1500_CR2","doi-asserted-by":"publisher","first-page":"S247","DOI":"10.1017\/S0031182004005190","volume":"129","author":"R Bock","year":"2004","unstructured":"Bock, R., Jackson, L., De Vos, A., & Jorgensen, W. (2004). Babesiosis of cattle. Parasitology, 129(Suppl), S247-269.","journal-title":"Parasitology"},{"issue":"10","key":"1500_CR3","doi-asserted-by":"publisher","first-page":"1504","DOI":"10.2174\/092986712799828355","volume":"19","author":"J Mosqueda","year":"2012","unstructured":"Mosqueda, J., Olvera-Ram\u00edrez, A., Aguilar-Tipacam\u00fa, G., & Cant\u00f3, G. J. (2012). Current advances in detection and treatment of babesiosis. Current Medicinal Chemistry, 19(10), 1504\u20131518.","journal-title":"Current Medicinal Chemistry"},{"key":"1500_CR4","doi-asserted-by":"publisher","first-page":"622","DOI":"10.1128\/CMR.16.4.622-636.2003","volume":"16","author":"A Zintl","year":"2003","unstructured":"Zintl, A., Mulcahy, G., Skerrett, H. E., Taylor, S. M., & Gray, J. S. (2003). Babesia divergens, a bovine blood parasite of veterinary and zoonotic importance. Clinical Microbiology Reviews, 16, 622\u2013636.","journal-title":"Clinical Microbiology Reviews"},{"key":"1500_CR5","doi-asserted-by":"publisher","first-page":"127","DOI":"10.1080\/00034983.1983.11811686","volume":"77","author":"CA Homewood","year":"1983","unstructured":"Homewood, C. A., & Neame, K. D. (1983). Conversion of glucose to lactate by intraerythrocytic Plasmodium berghei. Annals Of Tropical Medicine And Parasitology, 77, 127\u2013129.","journal-title":"Annals Of Tropical Medicine And Parasitology"},{"key":"1500_CR6","doi-asserted-by":"publisher","first-page":"235","DOI":"10.1016\/S0166-6851(97)00140-0","volume":"90","author":"MS Gomez","year":"1997","unstructured":"Gomez, M. S., Piper, R. C., Hunsaker, L. A., Royer, R. E., Deck, L. M., Makler, M. T., & Vander Jagt, D. L. (1997). Substrate and cofactor specificity and selective inhibition of lactate dehydrogenase from the malarial parasite P. falciparum. Molecular and Biochemical Parasitology, 90, 235\u2013246.","journal-title":"Molecular and Biochemical Parasitology"},{"key":"1500_CR7","doi-asserted-by":"publisher","first-page":"665","DOI":"10.1007\/PL00008549","volume":"86","author":"V Razakantoanina","year":"2000","unstructured":"Razakantoanina, V., Phung, N. K. P., & Jaureguiberry, G. (2000). Antimalarial activity of new gossypol derivatives. Parasitology Research, 86, 665\u2013668.","journal-title":"Parasitology Research"},{"issue":"12","key":"1500_CR8","doi-asserted-by":"publisher","DOI":"10.3389\/fcimb.2022.870852","volume":"19","author":"L He","year":"2022","unstructured":"He, L., Bastos, R. G., Yu, L., Laughery, J. M., & Suarez, C. E. (2022). Lactate dehydrogenase as a potential therapeutic drug target to control Babesia bigemina. Frontiers in Cellular and Infection Microbiology, 19(12), Article 870852.","journal-title":"Frontiers in Cellular and Infection Microbiology"},{"key":"1500_CR9","doi-asserted-by":"publisher","first-page":"912","DOI":"10.1038\/nsb1196-912","volume":"3","author":"CR Dunn","year":"1996","unstructured":"Dunn, C. R., Banfield, M. J., Barker, J. J., Higham, C. W., Moreton, K. M., Turgut-Balik, D., Brady, R. L., & Holbrook, J. J. (1996). The structure of lactate dehydrogenase from Plasmodium falciparum reveals a new target for anti-malarial design. Nature Structural Biology, 3, 912\u2013915.","journal-title":"Nature Structural Biology"},{"issue":"1","key":"1500_CR10","doi-asserted-by":"publisher","first-page":"23","DOI":"10.1016\/S0166-6851(01)00360-7","volume":"118","author":"C Dando","year":"2001","unstructured":"Dando, C., Schroeder, E. R., Hunsaker, L. A., Deck, L. M., Royer, R. E., Zhou, X., Parmley, S. F., & Vander Jagt, D. L. (2001). The kinetic properties and sensitivities to inhibitors of lactate dehydrogenases (LDH1 and LDH2) from Toxoplasma gondii: Comparisons with pLDH from Plasmodium falciparum. Molecular and Biochemical Parasitology, 118(1), 23\u201332.","journal-title":"Molecular and Biochemical Parasitology"},{"key":"1500_CR11","doi-asserted-by":"publisher","first-page":"165","DOI":"10.1016\/j.molbiopara.2004.03.009","volume":"136","author":"S Bork","year":"2004","unstructured":"Bork, S., Okamura, M., Boonchit, S., Hirata, H., Yokoyama, N., & Igarashi, I. (2004). Identification of Babesia bovis L-lactate dehydrogenase as a potential chemotherapeutical target against bovine babesiosis. Molecular and Biochemical Parasitology, 136, 165\u2013172.","journal-title":"Molecular and Biochemical Parasitology"},{"issue":"4","key":"1500_CR12","doi-asserted-by":"publisher","first-page":"879","DOI":"10.1021\/bi035108g","volume":"43","author":"KL Kavanagh","year":"2004","unstructured":"Kavanagh, K. L., Elling, R. A., & Wilson, D. K. (2004). Structure of Toxoplasma gondii LDH1: Active-site differences from human lactate dehydrogenases and the structural basis for efficient APAD+ use. Biochemistry, 43(4), 879\u2013889.","journal-title":"Biochemistry"},{"issue":"49","key":"1500_CR13","doi-asserted-by":"publisher","first-page":"16221","DOI":"10.1021\/bi051416y","volume":"44","author":"A Chaikuad","year":"2005","unstructured":"Chaikuad, A., Fairweather, V., Conners, R., Joseph-Horne, T., Turgut-Balik, D., & Brady, R. L. (2005). Structure of lactate dehydrogenase from Plasmodium vivax: Complexes with NADH and APADH. Biochemistry, 44(49), 16221\u201316228.","journal-title":"Biochemistry"},{"key":"1500_CR14","doi-asserted-by":"publisher","first-page":"256","DOI":"10.1007\/s12033-016-9924-3","volume":"58","author":"B Nural","year":"2016","unstructured":"Nural, B., Erdemir, A., Mutlu, O., Yakarsonmez, S., Danis, O., Topuzogullari, M., & Turgut-Balik, D. (2016). Biochemical and in silico characterization of recombinant L-lactate dehydrogenase of Theileria annulata. Molecular Biotechnology, 58, 256\u2013267.","journal-title":"Molecular Biotechnology"},{"key":"1500_CR15","doi-asserted-by":"publisher","DOI":"10.3389\/fcimb.2021.790101","volume":"11","author":"L Yu","year":"2022","unstructured":"Yu, L., Liu, Q., Luo, W., Zhao, J., Alzan, H. F., & He, L. (2022). The structural basis of Babesia orientalis lactate dehydrogenase. Frontiers in Cellular and Infection Microbiology, 11, Article 790101.","journal-title":"Frontiers in Cellular and Infection Microbiology"},{"key":"1500_CR16","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.02304","volume":"3","author":"JI Boucher","year":"2014","unstructured":"Boucher, J. I., Jacobowitz, J. R., Beckett, B. C., Classen, S., & Theobald, D. L. (2014). An atomic-resolution view of neofunctionalization in the evolution of apicomplexan lactate dehydrogenases. eLife, 3, Article e02304.","journal-title":"eLife"},{"key":"1500_CR17","doi-asserted-by":"publisher","DOI":"10.1007\/s00436-024-08433-5","volume":"124","author":"SM Bostancioglu","year":"2025","unstructured":"Bostancioglu, S. M., & Mutlu, O. (2025). Exploring novel inhibitors for Babesia bigemina lactate dehydrogenase: A computational structural biology perspective. Parasitology Research, 124, Article 1.","journal-title":"Parasitology Research"},{"issue":"D1","key":"1500_CR18","doi-asserted-by":"publisher","first-page":"D418","DOI":"10.1093\/nar\/gkac993","volume":"51","author":"T Paysan-Lafosse","year":"2023","unstructured":"Paysan-Lafosse, T., Blum, M., Chuguransky, S., Grego, T., Pinto, B. L., Salazar, G. A., Bileschi, M. L., Bork, P., Bridge, A., Colwell, L., Gough, J., Haft, D. H., Letuni\u0107, I., Marchler-Bauer, A., Mi, H., Natale, D. A., Orengo, C. A., Pandurangan, A. P., Rivoire, C., \u2026 Bateman, A. (2023). Interpro in 2022. Nucleic Acids Research, 51(D1), D418\u2013D427.","journal-title":"Nucleic Acids Research"},{"key":"1500_CR19","doi-asserted-by":"publisher","first-page":"W521","DOI":"10.1093\/nar\/gkae241","volume":"52","author":"F Madeira","year":"2024","unstructured":"Madeira, F., Madhusoodanan, N., Lee, J., Eusebi, A., Niewielska, A., Tivey, A. R. N., Lopez, R., & Butcher, S. (2024). The EMBL-EBI job dispatcher sequence analysis tools framework in 2024. Nucleic Acids Research, 52, W521\u2013W525.","journal-title":"Nucleic Acids Research"},{"key":"1500_CR20","doi-asserted-by":"publisher","first-page":"305","DOI":"10.1093\/bioinformatics\/15.4.305","volume":"15","author":"P Gouet","year":"1999","unstructured":"Gouet, P., Courcelle, E., Stuart, D. I., & Metoz, F. (1999). ESPript: Analysis of multiple sequence alignments in PostScript. Bioinformatics, 15, 305\u2013308.","journal-title":"Bioinformatics"},{"key":"1500_CR21","doi-asserted-by":"publisher","first-page":"732","DOI":"10.1016\/j.bbapap.2019.05.006","volume":"1867","author":"S Yakarsonmez","year":"2019","unstructured":"Yakarsonmez, S., Cengiz, E. C., Mutlu, O., & Turgut-Balik, D. (2019). Functional analyses of dipeptide and pentapeptide insertions on Theileria annulata enolase by site-directed mutagenesis and in silico approaches. Biochimica et Biophysica Acta, 1867, 732\u2013739.","journal-title":"Biochimica et Biophysica Acta"},{"key":"1500_CR22","doi-asserted-by":"publisher","DOI":"10.1016\/j.pep.2022.106187","volume":"202","author":"C Ayg\u00fcn","year":"2023","unstructured":"Ayg\u00fcn, C., Kocer, S., Dan\u0131\u015f, \u00d6., Cubuk, S., & Mutlu, O. (2023). Heterologous expression, purification, and partial characterisation of the apicoplast protein 3-oxoacyl-[acyl-carrier-protein] reductase from Toxoplasma gondii. Protein Expression and Purification, 202, Article 106187.","journal-title":"Protein Expression and Purification"},{"issue":"4","key":"1500_CR23","doi-asserted-by":"publisher","first-page":"1149","DOI":"10.1007\/s11030-019-10018-9","volume":"24","author":"S Yakarsonmez","year":"2020","unstructured":"Yakarsonmez, S., Danis, O., Mutlu, O., Topuzogullari, M., Sariyer, E., Yuce-Dursun, B., & Turgut-Balik, D. (2020). Discovery and evaluation of inhibitory activity and mechanism of arylcoumarin derivatives on Theileria annulata enolase by in vitro and molecular docking studies. Molecular Diversity, 24(4), 1149\u20131164.","journal-title":"Molecular Diversity"},{"key":"1500_CR24","doi-asserted-by":"publisher","first-page":"2738","DOI":"10.1111\/j.1742-4658.2007.05808.x","volume":"274","author":"DK Shoemark","year":"2007","unstructured":"Shoemark, D. K., Cliff, M. J., Sessions, R. B., & Clarke, A. R. (2007). Enzymatic properties of the lactate dehydrogenase enzyme from Plasmodium falciparum. The FEBS Journal, 274, 2738\u20132748.","journal-title":"The FEBS Journal"},{"key":"1500_CR25","doi-asserted-by":"publisher","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","volume":"72","author":"M Bradford","year":"1976","unstructured":"Bradford, M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72, 248\u2013254.","journal-title":"Analytical Biochemistry"},{"key":"1500_CR26","doi-asserted-by":"publisher","first-page":"4667","DOI":"10.1021\/bi00519a023","volume":"20","author":"K Gekko","year":"1981","unstructured":"Gekko, K., & Timasheff, S. N. (1981). Mechanism of protein stabilization by glycerol: Preferential hydration in glycerol-water mixtures. Biochemistry, 20, 4667\u20134676.","journal-title":"Biochemistry"},{"issue":"4","key":"1500_CR27","doi-asserted-by":"publisher","first-page":"480","DOI":"10.1021\/bi00892a002","volume":"3","author":"WW Cleland","year":"1964","unstructured":"Cleland, W. W. (1964). Dithiothreitol, a new protective reagent for SH groups. Biochemistry, 3(4), 480\u2013482.","journal-title":"Biochemistry"},{"key":"1500_CR28","doi-asserted-by":"publisher","first-page":"71","DOI":"10.1016\/j.ijbiomac.2021.02.144","volume":"179","author":"L Tian","year":"2021","unstructured":"Tian, L., Zhou, J., Lv, Q., Liu, F., Yang, T., Zhang, X., Xu, M., & Rao, Z. (2021). Rational engineering of the Plasmodium falciparum L-lactate dehydrogenase loop involved in catalytic proton transfer to improve chiral 2-hydroxybutyric acid production. International Journal of Biological Macromolecules, 179, 71\u201379.","journal-title":"International Journal of Biological Macromolecules"},{"key":"1500_CR29","doi-asserted-by":"publisher","first-page":"13669","DOI":"10.1096\/fj.201901259R","volume":"33","author":"L Yu","year":"2019","unstructured":"Yu, L., Shen, Z., Liu, Q., Zhan, X., Luo, X., An, X., Sun, Y., Li, M., Wang, S., Nie, Z., Ao, Y., Zhao, Y., Peng, G., Mamoun, C. B., He, L., & Zhao, J. (2019). Crystal structures of Babesia microti lactate dehydrogenase BmLDH reveal a critical role for Arg99 in catalysis. FASEB Journal, 33, 13669\u201313682.","journal-title":"FASEB Journal"},{"key":"1500_CR30","doi-asserted-by":"publisher","first-page":"418","DOI":"10.1007\/s10528-009-9322-7","volume":"48","author":"L Kuang","year":"2010","unstructured":"Kuang, L., Zheng, Y., Lin, Y., Xu, Y., Jin, S., Li, Y., Dong, F., & Jiang, Z. (2010). High-altitude adaptation of yak based on genetic variants and activity of lactate dehydrogenase-1. Biochemical Genetics, 48, 418\u2013427.","journal-title":"Biochemical Genetics"},{"key":"1500_CR31","doi-asserted-by":"publisher","first-page":"88","DOI":"10.1093\/clinchem\/27.1.88","volume":"27","author":"SM Pettit","year":"1981","unstructured":"Pettit, S. M., Nealon, D. A., & Henderson, A. R. (1981). Purification of lactate dehydrogenase isoenzyme-5 from human liver. Clinical Chemistry, 27, 88\u201393.","journal-title":"Clinical Chemistry"},{"key":"1500_CR32","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1005250","volume":"11","author":"H Zhang","year":"2015","unstructured":"Zhang, H., Guo, F., & Zhu, G. (2015). Cryptosporidium lactate dehydrogenase is associated with the parasitophorous vacuole membrane and is a potential target for developing therapeutics. PLoS Pathogens, 11, Article e1005250.","journal-title":"PLoS Pathogens"},{"key":"1500_CR33","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/S0166-6851(03)00170-1","volume":"131","author":"V Winter","year":"2003","unstructured":"Winter, V. (2003). Crystal structure of Plasmodium berghei lactate dehydrogenase indicates the unique structural differences of these enzymes are shared across the Plasmodium genus. Molecular And Biochemical Parasitology, 131, 1\u201310.","journal-title":"Molecular And Biochemical Parasitology"},{"key":"1500_CR34","doi-asserted-by":"publisher","first-page":"359","DOI":"10.1111\/j.1432-1033.1983.tb07662.x","volume":"135","author":"R Hensel","year":"1983","unstructured":"Hensel, R., Mayr, U., & Woenckhaus, C. (1983). Affinity labelling of the allosteric site of the L-lactate dehydrogenase of Lactobacillus casei. European Journal of Biochemistry, 135, 359\u2013365.","journal-title":"European Journal of Biochemistry"},{"issue":"2","key":"1500_CR35","doi-asserted-by":"publisher","first-page":"375","DOI":"10.1016\/0014-5793(88)80464-2","volume":"233","author":"H Matsuzawa","year":"1988","unstructured":"Matsuzawa, H., Machida, M., Kunai, K., Ito, Y., & Ohta, T. (1988). Identification of an allosteric site residue of a fructose 1,6-bisphosphate-dependent L-lactate dehydrogenase of Thermus caldophilus GK24: Production of a non-allosteric form by protein engineering. FEBS Letters, 233(2), 375\u2013378.","journal-title":"FEBS Letters"},{"key":"1500_CR36","doi-asserted-by":"publisher","first-page":"31550","DOI":"10.1074\/jbc.M114.599092","volume":"289","author":"Y Ikehara","year":"2014","unstructured":"Ikehara, Y., Arai, K., Furukawa, N., Ohno, T., Miyake, T., Fushinobu, S., Nakajima, M., Miyanaga, A., & Taguchi, H. (2014). The core of allosteric motion in Thermus caldophilus L-lactate dehydrogenase. Journal of Biological Chemistry, 289, 31550\u201331564.","journal-title":"Journal of Biological Chemistry"},{"issue":"1","key":"1500_CR37","doi-asserted-by":"publisher","first-page":"21","DOI":"10.1006\/jmbi.1993.1122","volume":"230","author":"S Iwata","year":"1993","unstructured":"Iwata, S., & Ohta, T. (1993). Molecular basis of allosteric activation of bacterial L-lactate dehydrogenase. Journal of Molecular Biology, 230(1), 21\u201327.","journal-title":"Journal of Molecular Biology"},{"key":"1500_CR38","doi-asserted-by":"publisher","first-page":"681","DOI":"10.1002\/prot.22597","volume":"78","author":"K Arai","year":"2010","unstructured":"Arai, K., Ishimitsu, T., Fushinobu, S., Uchikoba, H., Matsuzawa, H., & Taguchi, H. (2010). Active and inactive state structures of unliganded Lactobacillus casei allosteric L-lactate dehydrogenase. Proteins: Structure, Function, and Bioinformatics, 78, 681\u2013694.","journal-title":"Proteins: Structure, Function, and Bioinformatics"},{"key":"1500_CR39","doi-asserted-by":"publisher","first-page":"825","DOI":"10.1007\/s00239-001-0088-8","volume":"54","author":"D Madern","year":"2002","unstructured":"Madern, D. (2002). Molecular evolution within the L-malate and L-lactate dehydrogenase super-family. Journal of Molecular Evolution, 54, 825\u2013840.","journal-title":"Journal of Molecular Evolution"},{"key":"1500_CR40","doi-asserted-by":"publisher","first-page":"23","DOI":"10.1016\/j.biochi.2022.03.008","volume":"199","author":"LG Iacovino","year":"2022","unstructured":"Iacovino, L. G., Rossi, M., Di Stefano, G., Rossi, V., Binda, C., Brigotti, M., Tomaselli, F., Pasti, A. P., Dal Piaz, F., Cerini, S., & Hochkoeppler, A. (2022). Allosteric transitions of rabbit skeletal muscle lactate dehydrogenase induced by pH-dependent dissociation of the tetrameric enzyme. Biochimie, 199, 23\u201335.","journal-title":"Biochimie"},{"key":"1500_CR41","doi-asserted-by":"crossref","unstructured":"Pasti, A. P., Rossi, V., Di Stefano, G., Brigotti, M. and Hochkoeppler, A. (2022) Human lactate dehydrogenase A undergoes allosteric transitions under pH conditions inducing the dissociation of the tetrameric enzyme. Biosci.\u00a0Rep. 42(1), BSR20212654.","DOI":"10.1042\/BSR20212654"}],"container-title":["Molecular Biotechnology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s12033-025-01500-x.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s12033-025-01500-x","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s12033-025-01500-x.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,5,26]],"date-time":"2026-05-26T11:45:39Z","timestamp":1779795939000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s12033-025-01500-x"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,9,10]]},"references-count":41,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2026,5]]}},"alternative-id":["1500"],"URL":"https:\/\/doi.org\/10.1007\/s12033-025-01500-x","relation":{},"ISSN":["1073-6085","1559-0305"],"issn-type":[{"value":"1073-6085","type":"print"},{"value":"1559-0305","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,9,10]]},"assertion":[{"value":"18 March 2025","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"13 August 2025","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"10 September 2025","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"The authors declare no conflict of interest.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Conflict of interest"}},{"value":"This study does not raise any ethical concerns.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethical approval"}}]}}